Anti-Anopheles gambiae Alpha Amylase [AgAmy1] Antibody

This rabbit IgG polyclonal antibody was generated against a 20 kDa peptide corresponding to the C-terminal region of Anopheles gambiae Alpha Amylase 1 and recognizes A. gambiae Alpha Amylase 1.


  • Reacts with A. gamiae Amylase 1
  • Useful in R&D involving Anopheles, for identification and validation of targets for insect control by - d-endotoxins, and other biochemical/biological methods
  • Several species of Anopheles are disease vectors (malaria, canine heartworm, filariasis, O’nyong’nyong)
  • Recommended for Western Blot, Immunofluorescence, Immunohistochemistry and ELISA applications

a-Amylase also known as 1,4-a-D-Glucan glucanohydrolase; EC is a protein that hydrolyses alpha bonds of large, alpha-linked polysaccharides, and releases maltose from starch.

From the laboratory of Michael J. Adang, PhD, University of Georgia.

The Investigator's Annexe Part of The Investigator's Annexe program.

Catalog Number Product DataSheet Size AVAILABILITY Price Qty
Anti-Anopheles gambiae Alpha Amylase [AgAmy1] Antibody
50uL Currently unavailable
Regular Price:$375.00
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Product Type: Antibody
Antigen: alpha-amylase from A. gambiae
Accession ID: P04745
Molecular Weight: 70 kDa
Isotype: IgG
Clonality: Polyclonal
Clone Name: Anti-AgAmy1
Reactivity: A. gambiae. Very likely other members of the Anopheles genus, less likely Culex. Possibly, other insects/particularly mosquitoes
Immunogen: Peptide
Species Immunized: NZW Rabbit
Epitope: C-terminal region (20 kDa peptide)
Purification Method: Sepharose beads/ethanolamine buffer, pH 8
Buffer: Na2CO3/NaHCO3, pH 9.6
Tested Applications: WB, IF, IHC, ELISA
Storage: -80C
Shipped: Dry ice

From the laboratory of Michael J. Adang, PhD, University of Georgia.
  1. Zhang, Q., Hua, G., Bayyareddy, K., and Adang, M.J. 2013. Analyses of a-amylase and a-glucosidase in the malaria vector Anopheles gambiae as receptors of Cry11Ba toxins of Bacillus thuringiensis subsp. jegethesan. Insect Biochem. Mole. Biol. 31:907-915.
  2. Bayyareddy K1, Zhu X, Orlando R, Adang MJ. Proteome analysis of Cry4Ba toxin-interacting Aedes aegypti lipid rafts using geLC-MS/MS. J Proteome Res. 2012 Dec 7;11(12):5843-55.
  3. Bayyareddy K1, Andacht TM, Abdullah MA, Adang MJ. Proteomic identification of Bacillus thuringiensis subsp. israelensis toxin Cry4Ba binding proteins in midgut membranes from Aedes (Stegomyia) aegypti Linnaeus (Diptera, Culicidae) larvae. Insect Biochem Mol Biol. 2009 Apr;39(4):279-86.

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